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6-磷酸葡萄糖脱氢酶（G6PDH，EC 1.1.1.49）广泛存在于动物、植物、微生物及培养细胞中，作为磷酸戊糖途径的关键限速酶，其催化生成的NADPH不仅为细胞内还原性生物合成提供还原力，还通过维持谷胱甘肽的还原态水平，在保护细胞抵御氧化损伤中发挥核心作用，因此G6PDH活性可有效反映生物体的生物合成能力与抗氧化状态。该酶特异性催化6-磷酸葡萄糖氧化为6-磷酸葡萄糖酸内酯，同时将NADP⁺还原为NADPH。传统测定方法基于340 nm处直接监测NADPH的紫外吸收，但该法因NADPH摩尔消光系数较低而灵敏度不足，且易受样本中内源性紫外吸光物质的干扰。针对上述局限，本试剂盒提供一种简单、灵敏、快速的改良方案：酶促反应生成的NADPH在电子中介体介导下，与特异性显色探针WST-8反应，生成在450 nm处具有特征吸收峰的橙黄色甲臜产物，通过动力学模式连续监测单位时间内OD₄₅₀的初始线性增幅（ΔOD₄₅₀/min），即可精准计算出样本中G6PDH的酶活力大小。
Glucose‑6‑phosphate dehydrogenase (G6PDH, EC 1.1.1.49) is ubiquitously present in animals, plants, microorganisms, and cultured cells. As the key rate‑limiting enzyme of the pentose phosphate pathway, the NADPH generated by its catalysis not only provides reducing power for intracellular reductive biosynthesis, but also plays a central role in protecting cells against oxidative damage by maintaining the reduced state of glutathione. Therefore, G6PDH activity can effectively reflect the biosynthetic capacity and antioxidant status of organisms. This enzyme specifically catalyzes the oxidation of glucose‑6‑phosphate to 6‑phosphogluconolactone, while concomitantly reducing NADP⁺ to NADPH. Traditional assay methods are based on direct monitoring of NADPH absorption at 340 nm; however, this approach suffers from insufficient sensitivity due to the relatively low molar extinction coefficient of NADPH, and is also susceptible to interference from endogenous UV‑absorbing substances in samples. To overcome these limitations, this kit provides a simple, sensitive, and rapid improved protocol: the NADPH generated from the enzymatic reaction, mediated by an electron mediator, reacts with the specific chromogenic probe WST‑8 to produce an orange‑yellow formazan product with a characteristic absorption peak at 450 nm. By continuously monitoring the initial linear increase in absorbance at 450 nm per unit time (ΔOD₄₅₀/min) in kinetic mode, the G6PDH enzyme activity in the sample can be accurately calculated.
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